| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CD11b |
| Uniprot No | P11215 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 567-825aa |
| 氨基酸序列 | HSQRIAGSKLSPRLQYFGQSLSGGQDLTMDGLVDLTVGAQGHVLLLRSQPVLRVKAIMEFNPREVARNVFECNDQVVKGKEAGEVRVCLHVQKSTRDRLREGQIQSVVTYDLALDSGRPHSRAVFNETKNSTRRQTQVLGLTQTCETLKLQLPNCIEDPVSPIVLRLNFSLVGTPLSAFGNLRPVLAEDAQRLFTALFPFEKNCGNDNICQDDLSITFSFMSLDCLVVGGPREFNVTVTVRNDGEDSYRTQVTFFFPLD |
| 预测分子量 | 29 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于CD11b重组蛋白的3篇参考文献示例(内容基于典型研究归纳)：
1. **"Expression and functional characterization of recombinant CD11b/CD18 integrin in mammalian cells"**
- **作者**: Springer, T.A. 等
- **摘要**: 研究报道了在哺乳动物细胞(如HEK293)中重组表达CD11b/CD18(Mac-1)的方法，通过亲和层析纯化蛋白，并验证其与配体(如ICAM-1、纤维蛋白原)的结合活性，揭示了整合素在炎症反应中的分子机制。
2. **"Structural basis of CD11b activation in neutrophil adhesion and inflammation"**
- **作者**: Shimaoka, M. 等
- **摘要**: 通过晶体结构解析重组CD11b胞外域，揭示了其构象变化与激活机制，阐明了金属离子(如Mg²⁺)在配体结合中的关键作用，为靶向CD11b的抗炎药物设计提供依据。
3. **"Targeted delivery of nanoparticles to activated CD11b+ monocytes in sepsis"**
- **作者**: Hidalgo, G. 等
- **摘要**: 利用重组CD11b蛋白修饰纳米颗粒，实现特异性靶向活化的单核细胞/巨噬细胞，在脓毒症小鼠模型中验证了其递送效率和抗炎治疗效果。
*注：以上为示例性内容，实际文献需通过数据库(如PubMed)检索确认。*
CD11b, also known as integrin αM, is a key subunit of the heterodimeric transmembrane receptor Mac-1 (CD11b/CD18 or αMβ2 integrin). It plays a critical role in immune responses by mediating leukocyte adhesion, migration, and phagocytosis. Expressed predominantly on myeloid cells (monocytes, macrophages, neutrophils), CD11b interacts with ligands such as ICAM-1. fibrinogen, and complement component iC3b, facilitating cell-cell communication and inflammatory processes. Its involvement in immune regulation makes it a biomarker for immune cell activation and a therapeutic target in inflammatory diseases, cancer, and autoimmune disorders.
Recombinant CD11b proteins are engineered to study its structure-function relationships or develop targeted therapies. Produced using mammalian or insect expression systems (e.g., HEK293 or Sf9 cells), these proteins retain post-translational modifications critical for ligand binding. The recombinant form often includes the extracellular domain fused with tags (e.g., Fc or His-tag) for purification and detection. Researchers utilize them in binding assays, inhibitor screening, and structural studies (e.g., X-ray crystallography) to map interaction interfaces or design blocking antibodies. In drug development, CD11b-targeting biologics aim to modulate excessive inflammation or enhance immune surveillance. Recent studies also explore its role in modulating macrophage polarization, linking it to tissue repair and fibrosis. Despite progress, challenges remain in mimicking native conformational changes (e.g., activation from bent to extended states) in recombinant forms, necessitating advanced expression strategies. Overall, CD11b recombinant proteins serve as indispensable tools for dissecting immune mechanisms and advancing immunotherapies.
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